University of Illinois at Chicago
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The GTPase RaB26 links synaptic vesicles to the autophagy pathway

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journal contribution
posted on 2016-01-07, 00:00 authored by B. Binotti, N.J. Pavlos, D. Riedel, D. Wenzel, G. Vorbrüggen, A.M. Schalk, K. Kühnel, J. Boyken, C. Erck, H. Martens, J.J. Chua, R. Jahn
Small GTPases of the Rab family not only regulate target recognition in membrane traffic but also control other cellular functions such as cytoskeletal transport and autophagy. Here we show that Rab26 is specifically associated with clusters of synaptic vesicles in neurites. Overexpression of active but not of GDP-preferring Rab26 enhances vesicle clustering, which is particularly conspicuous for the EGFP-tagged variant, resulting in a massive accumulation of synaptic vesicles in neuronal somata without altering the distribution of other organelles. Both endogenous and induced clusters co-localize with autophagy-related proteins such as Atg16L1, LC3B and Rab33B but not with other organelles. Furthermore, Atg16L1 appears to be a direct effector of Rab26 and binds Rab26 in its GTP-bound form, albeit only with low affinity. We propose that Rab26 selectively directs synaptic and secretory vesicles into preautophagosomal structures, suggesting the presence of a novel pathway for degradation of synaptic vesicles.


National Health and Medical Research Council (NHMRC) 463911 CJ Martin Fellowship Nathan J Pavlos


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This Document is Protected by copyright and was first published by eLife Sciences Publications. All rights reserved. It is reproduced with permission. (CC)Copyright Binotti et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.


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